Phosphatidylinositol-binding clathrin assembly protein

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• 1-phosphatidylinositol binding Source: UniProtKB
• amyloid-beta binding Source: ARUK-UCL
• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• clathrin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.8

    "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
    Tebar F., Bohlander S.K., Sorkin A.
    Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
• clathrin heavy chain binding Source: BHF-UCLInferred from direct assayⁱ
  • Ref.8

    "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
    Tebar F., Bohlander S.K., Sorkin A.
    Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
• low-density lipoprotein particle receptor binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• phosphatidylinositol-4,5-bisphosphate binding Source: ARUK-UCL <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • Ref.25

    "CALM regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature."
    Miller S.E., Mathiasen S., Bright N.A., Pierre F., Kelly B.T., Kladt N., Schauss A., Merrifield C.J., Stamou D., Hoening S., Owen D.J.
    Dev. Cell 33:163-175(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• small GTPase binding Source: ARUK-UCLInferred from physical interactionⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• SNARE binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM."
    Miller S.E., Sahlender D.A., Graham S.C., Honing S., Robinson M.S., Peden A.A., Owen D.J.
    Cell 147:1118-1131(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH VAMP2; VAMP3 AND VAMP8.
• tau protein binding Source: Alzheimers_University_of_TorontoInferred from physical interactionⁱ
  • "Clathrin adaptor CALM/PICALM is associated with neurofibrillary tangles and is cleaved in Alzheimer's brains."
    Ando K., Brion J.P., Stygelbout V., Suain V., Authelet M., Dedecker R., Chanut A., Lacor P., Lavaur J., Sazdovitch V., Rogaeva E., Potier M.C., Duyckaerts C.
    Acta Neuropathol 125:861-878(2013) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• amyloid-beta clearance by transcytosis Source: ARUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• axonogenesis Source: Ensembl
• clathrin coat assembly Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.9

    "Effect of clathrin assembly lymphoid myeloid leukemia protein depletion on clathrin coat formation."
    Meyerholz A., Hinrichsen L., Groos S., Esk P.C., Brandes G., Ungewickell E.J.
    Traffic 6:1225-1234(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AP2A1 AND CLATHRIN.
• clathrin-coated pit assembly Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "Effect of clathrin assembly lymphoid myeloid leukemia protein depletion on clathrin coat formation."
    Meyerholz A., Hinrichsen L., Groos S., Esk P.C., Brandes G., Ungewickell E.J.
    Traffic 6:1225-1234(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AP2A1 AND CLATHRIN.
• clathrin-dependent endocytosis Source: Alzheimers_University_of_TorontoInferred from mutant phenotypeⁱ
  • "The PICALM protein plays a key role in iron homeostasis and cell proliferation."
    Scotland P.B., Heath J.L., Conway A.E., Porter N.B., Armstrong M.B., Walker J.A., Klebig M.L., Lavau C.P., Wechsler D.S.
    PLoS One 7:e44252-e44252(2012) [PubMed] [Europe PMC] [Abstract]
  • "Decreased CALM expression reduces Abeta42 to total Abeta ratio through clathrin-mediated endocytosis of gamma-secretase."
    Kanatsu K., Morohashi Y., Suzuki M., Kuroda H., Watanabe T., Tomita T., Iwatsubo T.
    Nat Commun 5:3386-3386(2014) [PubMed] [Europe PMC] [Abstract]
• dendrite morphogenesis Source: Ensembl
• endocytosis Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM."
    Miller S.E., Sahlender D.A., Graham S.C., Honing S., Robinson M.S., Peden A.A., Owen D.J.
    Cell 147:1118-1131(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH VAMP2; VAMP3 AND VAMP8.
• endosomal transport Source: BHF-UCLInferred from mutant phenotypeⁱ
  • Ref.9

    "Effect of clathrin assembly lymphoid myeloid leukemia protein depletion on clathrin coat formation."
    Meyerholz A., Hinrichsen L., Groos S., Esk P.C., Brandes G., Ungewickell E.J.
    Traffic 6:1225-1234(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AP2A1 AND CLATHRIN.
• hemopoiesis Source: Ensembl
• iron ion homeostasis Source: Alzheimers_University_of_TorontoInferred from mutant phenotypeⁱ
  • "The PICALM protein plays a key role in iron homeostasis and cell proliferation."
    Scotland P.B., Heath J.L., Conway A.E., Porter N.B., Armstrong M.B., Walker J.A., Klebig M.L., Lavau C.P., Wechsler D.S.
    PLoS One 7:e44252-e44252(2012) [PubMed] [Europe PMC] [Abstract]
• learning or memory Source: ARUK-UCLInferred from sequence or structural similarityⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• membrane bending Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • Ref.25

    "CALM regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature."
    Miller S.E., Mathiasen S., Bright N.A., Pierre F., Kelly B.T., Kladt N., Schauss A., Merrifield C.J., Stamou D., Hoening S., Owen D.J.
    Dev. Cell 33:163-175(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• modulation of age-related behavioral decline Source: ARUK-UCLInferred from sequence or structural similarityⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• negative regulation of gene expression Source: Alzheimers_University_of_TorontoInferred from mutant phenotypeⁱ
  • "The PICALM protein plays a key role in iron homeostasis and cell proliferation."
    Scotland P.B., Heath J.L., Conway A.E., Porter N.B., Armstrong M.B., Walker J.A., Klebig M.L., Lavau C.P., Wechsler D.S.
    PLoS One 7:e44252-e44252(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
• negative regulation of protein localization to cell surface Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "CALM, a clathrin assembly protein, influences cell surface GluR2 abundance."
    Harel A., Mattson M.P., Yao P.J.
    Neuromolecular Med 13:88-90(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein localization to plasma membrane Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "CALM, a clathrin assembly protein, influences cell surface GluR2 abundance."
    Harel A., Mattson M.P., Yao P.J.
    Neuromolecular Med 13:88-90(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of receptor-mediated endocytosis Source: BHF-UCLInferred from direct assayⁱ
  • Ref.8

    "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
    Tebar F., Bohlander S.K., Sorkin A.
    Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
• positive regulation of amyloid-beta formation Source: Alzheimers_University_of_TorontoInferred from mutant phenotypeⁱ
  • "Decreased CALM expression reduces Abeta42 to total Abeta ratio through clathrin-mediated endocytosis of gamma-secretase."
    Kanatsu K., Morohashi Y., Suzuki M., Kuroda H., Watanabe T., Tomita T., Iwatsubo T.
    Nat Commun 5:3386-3386(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
• positive regulation of GTPase activity Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of neuron death Source: Alzheimers_University_of_TorontoInferred from mutant phenotypeⁱ
  • "Clathrin adaptor CALM/PICALM is associated with neurofibrillary tangles and is cleaved in Alzheimer's brains."
    Ando K., Brion J.P., Stygelbout V., Suain V., Authelet M., Dedecker R., Chanut A., Lacor P., Lavaur J., Sazdovitch V., Rogaeva E., Potier M.C., Duyckaerts C.
    Acta Neuropathol 125:861-878(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription, DNA-templated Source: BHF-UCLInferred from direct assayⁱ
  • "Nucleocytoplasmic shuttling of endocytic proteins."
    Vecchi M., Polo S., Poupon V., van de Loo J.W., Benmerah A., Di Fiore P.P.
    J Cell Biol 153:1511-1517(2001) [PubMed] [Europe PMC] [Abstract]
• protein-containing complex assembly Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "The t(10;11)(p13;q14) in the U937 cell line results in the fusion of the AF10 gene and CALM, encoding a new member of the AP-3 clathrin assembly protein family."
    Dreyling M.H., Martinez-Climent J.A., Zheng M., Mao J., Rowley J.D., Bohlander S.K.
    Proc. Natl. Acad. Sci. U.S.A. 93:4804-4809(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION, TISSUE SPECIFICITY, VARIANTS CYS-578 AND GLU-579.
• receptor internalization Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference."
    Huang F., Khvorova A., Marshall W., Sorkin A.
    J. Biol. Chem. 279:16657-16661(2004) [PubMed] [Europe PMC] [Abstract]
• receptor-mediated endocytosis Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
    Tebar F., Bohlander S.K., Sorkin A.
    Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
• regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_TorontoInferred from mutant phenotypeⁱ
  • "Decreased CALM expression reduces Abeta42 to total Abeta ratio through clathrin-mediated endocytosis of gamma-secretase."
    Kanatsu K., Morohashi Y., Suzuki M., Kuroda H., Watanabe T., Tomita T., Iwatsubo T.
    Nat Commun 5:3386-3386(2014) [PubMed] [Europe PMC] [Abstract]
• regulation of endocytosis Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Evidence for CALM in directing VAMP2 trafficking."
    Harel A., Wu F., Mattson M.P., Morris C.M., Yao P.J.
    Traffic 9:417-429(2008) [PubMed] [Europe PMC] [Abstract]
• regulation of protein localization Source: BHF-UCLInferred from direct assayⁱ
  • Ref.8

    "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
    Tebar F., Bohlander S.K., Sorkin A.
    Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
• regulation of vesicle size Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • Ref.25

    "CALM regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature."
    Miller S.E., Mathiasen S., Bright N.A., Pierre F., Kelly B.T., Kladt N., Schauss A., Merrifield C.J., Stamou D., Hoening S., Owen D.J.
    Dev. Cell 33:163-175(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• synaptic vesicle budding from presynaptic endocytic zone membrane Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• synaptic vesicle maturation Source: Alzheimers_University_of_Toronto
• vesicle budding from membrane Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • Ref.25

    "CALM regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature."
    Miller S.E., Mathiasen S., Bright N.A., Pierre F., Kelly B.T., Kladt N., Schauss A., Merrifield C.J., Stamou D., Hoening S., Owen D.J.
    Dev. Cell 33:163-175(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• vesicle cargo loading Source: Alzheimers_University_of_TorontoInferred from mutant phenotypeⁱ
  • "Decreased CALM expression reduces Abeta42 to total Abeta ratio through clathrin-mediated endocytosis of gamma-secretase."
    Kanatsu K., Morohashi Y., Suzuki M., Kuroda H., Watanabe T., Tomita T., Iwatsubo T.
    Nat Commun 5:3386-3386(2014) [PubMed] [Europe PMC] [Abstract]
• vesicle-mediated transport Source: ProtIncTraceable author statementⁱ
  • Ref.1

    "The t(10;11)(p13;q14) in the U937 cell line results in the fusion of the AF10 gene and CALM, encoding a new member of the AP-3 clathrin assembly protein family."
    Dreyling M.H., Martinez-Climent J.A., Zheng M., Mao J., Rowley J.D., Bohlander S.K.
    Proc. Natl. Acad. Sci. U.S.A. 93:4804-4809(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION, TISSUE SPECIFICITY, VARIANTS CYS-578 AND GLU-579.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Sites

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• clathrin binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
    Tebar F., Bohlander S.K., Sorkin A.
    Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
• clathrin heavy chain binding Source: BHF-UCLInferred from direct assayⁱ
  • Ref.8

    "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
    Tebar F., Bohlander S.K., Sorkin A.
    Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
• low-density lipoprotein particle receptor binding Source: ARUK-UCLInferred from physical interactionⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• small GTPase binding Source: ARUK-UCLInferred from physical interactionⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat Neurosci 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• SNARE binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM."
    Miller S.E., Sahlender D.A., Graham S.C., Honing S., Robinson M.S., Peden A.A., Owen D.J.
    Cell 147:1118-1131(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH VAMP2; VAMP3 AND VAMP8.
• tau protein binding Source: Alzheimers_University_of_TorontoInferred from physical interactionⁱ
  • "Clathrin adaptor CALM/PICALM is associated with neurofibrillary tangles and is cleaved in Alzheimer's brains."
    Ando K., Brion J.P., Stygelbout V., Suain V., Authelet M., Dedecker R., Chanut A., Lacor P., Lavaur J., Sazdovitch V., Rogaeva E., Potier M.C., Duyckaerts C.
    Acta Neuropathol 125:861-878(2013) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 5 described isoforms and 11 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN 
        60         70         80         90        100
EMNVNIPQLA DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR 
       110        120        130        140        150
NTLFNLSNFL DKSGLQGYDM STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR 
       160        170        180        190        200
GADGVMRTMN TEKLLKTVPI IQNQMDALLD FNVNSNELTN GVINAAFMLL 
       210        220        230        240        250
FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF LTRMTRISEF 
       260        270        280        290        300
LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT 
       310        320        330        340        350
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP 
       360        370        380        390        400
HTSLTTAASP VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT 
       410        420        430        440        450
FHPSVHPMST ASQVASTWGD PFSATVDAVD DAIPSLNPFL TKSSGDVHLS 
       460        470        480        490        500
ISSDVSTFTT RTPTHEMFVG FTPSPVAQPH PSAGLNVDFE SVFGNKSTNV 
       510        520        530        540        550
IVDSGGFDEL GGLLKPTVAS QNQNLPVAKL PPSKLVSDDL DSSLANLVGN 
       560        570        580        590        600
LGIGNGTTKN DVNWSQPGEK KLTGGSNWQP KVAPTTAWNA ATMAPPVMAY 
       610        620        630        640        650
PATTPTGMIG YGIPPQMGSV PVMTQPTLIY SQPVMRPPNP FGPVSGAQIQ 

FM                                                     

        10         20         30         40         50
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN 
        60         70         80         90        100
EMNVNIPQLA DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR 
       110        120        130        140        150
NTLFNLSNFL DKSGLQGYDM STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR 
       160        170        180        190        200
GADGVMRTMN TEKLLKTVPI IQNQMDALLD FNVNSNELTN GVINAAFMLL 
       210        220        230        240        250
FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF LTRMTRISEF 
       260        270        280        290        300
LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT 
       310        320        330        340        350
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP 
       360        370        380        390        400
HTSLTTAASP VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT 
       410        420        430        440        450
FHPSVHPMST ASQVASTWGD PFSATVDAVD DAIPSLNPFL TKSSGDVHLS 
       460        470        480        490        500
ISSDVSTFTT RTPTHEMFVG FTPSPVAQPH PSAGLNVDFE SVFGNKSTNV 
       510        520        530        540        550
IVDSGGFDEL GGLLKPTVAS QNQNLPVAKL PPSKLVSDDL DSSLANLVGN 
       560        570        580        590        600
LGIGNGTTKN DVNWSQPGEK KLTGGSNWQP KVAPTTAWNA ATMPPQMGSV 
       610        620        630 
PVMTQPTLIY SQPVMRPPNP FGPVSGAQIQ FM                    

        10         20         30         40         50
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN 
        60         70         80         90        100
EMNVNIPQLA DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR 
       110        120        130        140        150
NTLFNLSNFL DKSGLQGYDM STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR 
       160        170        180        190        200
GADGVMRTMN TEKLLKTVPI IQNQMDALLD FNVNSNELTN GVINAAFMLL 
       210        220        230        240        250
FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF LTRMTRISEF 
       260        270        280        290        300
LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT 
       310        320        330        340        350
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP 
       360        370        380        390        400
HTSLTTAASP VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT 
       410        420        430        440        450
FHPSVHPMST ASQVASTWGG FTPSPVAQPH PSAGLNVDFE SVFGNKSTNV 
       460        470        480        490        500
IVDSGGFDEL GGLLKPTVAS QNQNLPVAKL PPSKLVSDDL DSSLANLVGN 
       510        520        530        540        550
LGIGNGTTKN DVNWSQPGEK KLTGGSNWQP KVAPTTAWNA ATMNGMHFPQ 
       560        570        580        590        600
YAPPVMAYPA TTPTGMIGYG IPPQMGSVPV MTQPTLIYSQ PVMRPPNPFG 
       610
PVSGAQIQFM                                             

        10         20         30         40         50
MNVNIPQLAD SLFERTTNSS WVVVFKSLIT THHLMVYGNE RFIQYLASRN 
        60         70         80         90        100
TLFNLSNFLD KSGLQGYDMS TFIRRYSRYL NEKAVSYRQV AFDFTKVKRG 
       110        120        130        140        150
ADGVMRTMNT EKLLKTVPII QNQMDALLDF NVNSNELTNG VINAAFMLLF 
       160        170        180        190        200
KDAIRLFAAY NEGIINLLEK YFDMKKNQCK EGLDIYKKFL TRMTRISEFL 
       210        220        230        240        250
KVAEQVGIDR GDIPDLSQAP SSLLDALEQH LASLEGKKIK DSTAASRATT 
       260        270        280        290        300
LSNAVSSLAS TGLSLTKVDE REKQAALEEE QARLKALKEQ RLKELAKKPH 
       310        320        330        340        350
TSLTTAASPV STSAGGIMTA PAIDIFSTPS SSNSTSKLPN DLLDLQQPTF 
       360        370        380        390        400
HPSVHPMSTA SQVASTWGGF TPSPVAQPHP SAGLNVDFES VFGNKSTNVI 
       410        420        430        440        450
VDSGGFDELG GLLKPTVASQ NQNLPVAKLP PSKLVSDDLD SSLANLVGNL 
       460        470        480        490        500
GIGNGTTKND VNWSQPGEKK LTGGSNWQPK VAPTTAWNAA TMAPPVMAYP 
       510        520        530        540        550
ATTPTGMIGY GIPPQMGSVP VMTQPTLIYS QPVMRPPNPF GPVSGAQIQF 

M                                                      

        10         20         30         40         50
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN 
        60         70         80         90        100
EMNVNIPQLA DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR 
       110        120        130        140        150
NTLFNLSNFL DKSGLQGYDM STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR 
       160        170        180        190        200
GADGVMRTMN TEKLLKTVPI IQNQMDALLD FNVNSNELTN GVINAAFMLL 
       210        220        230        240        250
FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF LTRMTRISEF 
       260        270        280        290        300
LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT 
       310        320        330        340        350
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP 
       360        370        380        390        400
HTSLTTAASP VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT 
       410        420        430        440        450
FHPSVHPMST ASQVASTWGD AVDDAIPSLN PFLTKSSGDV HLSISSDVST 
       460        470        480        490        500
FTTRTPTHEM FVGFTPSPVA QPHPSAGLNV DFESVFGNKS TNVIVDSGGF 
       510        520        530        540        550
DELGGLLKPT VASQNQNLPV AKLPPSKLVS DDLDSSLANL VGNLGIGNGT 
       560        570        580        590        600
TKNDVNWSQP GEKKLTGGSN WQPKVAPTTA WNAATMAPPV MAYPATTPTG 
       610        620        630        640 
MIGYGIPPQM GSVPVMTQPT LIYSQPVMRP PNPFGPVSGA QIQFM      

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ